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CAZyme Information: MGYG000003569_01649

You are here: Home > Sequence: MGYG000003569_01649

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Treponema_D sp900769975
Lineage Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900769975
CAZyme ID MGYG000003569_01649
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
369 41308.86 7.1694
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003569 3076540 MAG Fiji Oceania
Gene Location Start: 12096;  End: 13205  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003569_01649.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0739 NlpD 6.43e-47 128 364 1 257
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 8.12e-43 269 364 1 96
Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
cd12797 M23_peptidase 4.73e-38 271 355 1 85
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
PRK11649 PRK11649 1.27e-22 265 364 307 406
putative peptidase; Provisional
COG4942 EnvC 2.28e-13 273 365 323 415
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNL98185.1 1.16e-130 26 368 12 349
QQA00877.1 1.28e-122 122 367 83 328
QSI02996.1 1.38e-122 57 369 15 322
QTQ15681.1 2.47e-113 43 368 5 301
QTQ12325.1 2.47e-113 43 368 5 301

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3SLU_A 1.09e-24 230 364 208 338
Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A 1.56e-24 230 364 228 358
1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
4RNY_A 8.89e-23 235 364 184 313
Structureof Helicobacter pylori Csd3 from the orthorhombic crystal [Helicobacter pylori 26695],4RNY_B Structure of Helicobacter pylori Csd3 from the orthorhombic crystal [Helicobacter pylori 26695],4RNZ_A Structure of Helicobacter pylori Csd3 from the hexagonal crystal [Helicobacter pylori 26695]
5J1L_A 7.21e-20 271 364 65 160
Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_C Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_A Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_C Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
6UE4_A 3.93e-18 238 363 228 358
ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P44693 1.73e-17 245 364 322 442
Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
Q89AI9 8.25e-17 241 367 221 347
Uncharacterized metalloprotease bbp_296 OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=bbp_296 PE=3 SV=1
Q8K9M4 3.51e-16 249 364 269 384
Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1
O64046 3.64e-16 252 364 1564 1674
Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976 3.64e-16 252 364 1564 1674
SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.999959 0.000058 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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